NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568947361|ref|XP_006540705|]
View 

PREDICTED: insulin-like growth factor 1 receptor isoform X2 [Mus musculus]

Protein Classification

FU and PTKc_InsR_like domain-containing protein (domain architecture ID 12013544)

protein containing domains FU, Recep_L_domain, FN3, and PTKc_InsR_like

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
993-1301 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 566.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  993 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1072
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1073 GQPTLVIMELMTRGDLKSYLRSLRPEVEprlswnslrrpgwprtlrdslasvsqvlalkqNNLVLIPPSLSKMIQMAGEI 1152
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAE--------------------------------NNPGLGPPTLQKFIQMAAEI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1153 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFG 1232
Cdd:cd05032   129 ADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFG 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947361 1233 VVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1301
Cdd:cd05032   209 VVLWEMATLAEQPYQGLSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
Furin-like pfam00757
Furin-like cysteine rich region;
175-330 1.69e-65

Furin-like cysteine rich region;


:

Pssm-ID: 307072 [Multi-domain]  Cd Length: 143  Bit Score: 217.69  E-value: 1.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   175 PKECGDLCPGTLEEKPMCEKttinneyNYRCWTTNRCQKMCPSVCGKRaCTENNECCHPECLGSCHTPDDnTTCVACRHY 254
Cdd:pfam00757    1 NKECGDVCPGTMEKCHSCCN-------NGYCWGPGHCQKVCPEQCKKR-CTKPGECCHEQCLGGCTGPND-SDCLACRHF 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947361   255 YYKGVCVPACPPGTYRFeGWRCVDRDFCaniPNAESSDSDGFVIHDDECMQECPSGFIRNSTQSMYCIPCEGPCPK 330
Cdd:pfam00757   72 NDEGTCVDTCPPGTYQF-GWRCVTFKEC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNSRKCEPCEGLCPK 143
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
353-466 8.61e-38

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


:

Pssm-ID: 334353  Cd Length: 110  Bit Score: 137.36  E-value: 8.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   353 GCTILKGNLLINIRRGNNIaSELENFMGLIEVVTGYVKIRHShALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQL 432
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGD-SELLSFLSTVEEITGYLLIANT-NLVSLSFLPNLRIIRGRNLFEDNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568947361   433 WDWNHRNLTvrSGKMYFAFNPKLCVSEIYRMEEV 466
Cdd:pfam01030   79 GLPSLKEIT--SGGVYIHNNPKLCYSETEIDWKL 110
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
51-159 1.36e-33

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


:

Pssm-ID: 334353  Cd Length: 110  Bit Score: 125.03  E-value: 1.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361    51 NCTVIEGFLHILLISKAEDYRSYR-FPKLTVITEYLLLFRVAgLESLgDLFPNLTVIRGWKLFY-NYALVIFEMTNLKDI 128
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGDSELLSfLSTVEEITGYLLIANTN-LVSL-SFLPNLRIIRGRNLFEdNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 568947361   129 GLYNLRNITRGAIRIEKNADLCYLST-IDWSL 159
Cdd:pfam01030   79 GLPSLKEITSGGVYIHNNPKLCYSETeIDWKL 110
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
836-925 2.06e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  836 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYgGAKLNRLNPG-NYTARIQATSLSGN 914
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGtEYEFRVRAVNGGGE 82
                          90
                  ....*....|.
gi 568947361  915 GSWTDPVFFYV 925
Cdd:cd00063    83 SPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
494-607 1.21e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.88  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  494 LRFTSTTtwKNRIIITWHRyRPPDYRDLISFTVYYKEApfknvteydgqdacGSNSWNMVDVDLPPNKEgepgILLHGLK 573
Cdd:cd00063     7 LRVTDVT--STSVTLSWTP-PEDDGGPITGYVVEYREK--------------GSGDWKEVEVTPGSETS----YTLTGLK 65
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568947361  574 PWTQYAVYVKAVtltmveNDHIRGAKSEILYIRT 607
Cdd:cd00063    66 PGTEYEFRVRAV------NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
612-656 1.54e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 1.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947361  612 PSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDG 656
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD 45
 
Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
993-1301 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 566.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  993 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1072
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1073 GQPTLVIMELMTRGDLKSYLRSLRPEVEprlswnslrrpgwprtlrdslasvsqvlalkqNNLVLIPPSLSKMIQMAGEI 1152
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAE--------------------------------NNPGLGPPTLQKFIQMAAEI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1153 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFG 1232
Cdd:cd05032   129 ADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFG 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947361 1233 VVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1301
Cdd:cd05032   209 VVLWEMATLAEQPYQGLSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
1000-1296 8.83e-129

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 398.02  E-value: 8.83e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1000 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1079
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGE-GENTKIKVAVKTLKEGADEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1080 MELMTRGDLKSYLRSLRPeveprlswnslrrpgwprtlrdslasvsqvlalkqnnlvliPPSLSKMIQMAGEIADGMAYL 1159
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHKG-----------------------------------------KLTLKDLLSMALQIAKGMEYL 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1160 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIA 1239
Cdd:pfam07714  119 ESKNFVHRDLAARNILVTENLVVKISDFGLSRDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIF 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947361  1240 TLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 1296
Cdd:pfam07714  199 TLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMTQCWAYDPEDRPTFSELV 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1000-1299 1.13e-120

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 376.12  E-value: 1.13e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1000 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1079
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGK-GDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1080 MELMTRGDLKSYLRSLRPEVeprlswnslrrpgwprtlrdslasvsqvlalkqnnlvlipPSLSKMIQMAGEIADGMAYL 1159
Cdd:smart00221   80 MEYMPGGDLLDYLRKNRPKE----------------------------------------LSLSDLLSFALQIARGMEYL 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1160 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGkGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIA 1239
Cdd:smart00221  120 ESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF 198
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1240 TLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSI 1299
Cdd:smart00221  199 TLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
Furin-like pfam00757
Furin-like cysteine rich region;
175-330 1.69e-65

Furin-like cysteine rich region;


Pssm-ID: 307072 [Multi-domain]  Cd Length: 143  Bit Score: 217.69  E-value: 1.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   175 PKECGDLCPGTLEEKPMCEKttinneyNYRCWTTNRCQKMCPSVCGKRaCTENNECCHPECLGSCHTPDDnTTCVACRHY 254
Cdd:pfam00757    1 NKECGDVCPGTMEKCHSCCN-------NGYCWGPGHCQKVCPEQCKKR-CTKPGECCHEQCLGGCTGPND-SDCLACRHF 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947361   255 YYKGVCVPACPPGTYRFeGWRCVDRDFCaniPNAESSDSDGFVIHDDECMQECPSGFIRNSTQSMYCIPCEGPCPK 330
Cdd:pfam00757   72 NDEGTCVDTCPPGTYQF-GWRCVTFKEC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNSRKCEPCEGLCPK 143
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
353-466 8.61e-38

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


Pssm-ID: 334353  Cd Length: 110  Bit Score: 137.36  E-value: 8.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   353 GCTILKGNLLINIRRGNNIaSELENFMGLIEVVTGYVKIRHShALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQL 432
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGD-SELLSFLSTVEEITGYLLIANT-NLVSLSFLPNLRIIRGRNLFEDNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568947361   433 WDWNHRNLTvrSGKMYFAFNPKLCVSEIYRMEEV 466
Cdd:pfam01030   79 GLPSLKEIT--SGGVYIHNNPKLCYSETEIDWKL 110
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
51-159 1.36e-33

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


Pssm-ID: 334353  Cd Length: 110  Bit Score: 125.03  E-value: 1.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361    51 NCTVIEGFLHILLISKAEDYRSYR-FPKLTVITEYLLLFRVAgLESLgDLFPNLTVIRGWKLFY-NYALVIFEMTNLKDI 128
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGDSELLSfLSTVEEITGYLLIANTN-LVSL-SFLPNLRIIRGRNLFEdNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 568947361   129 GLYNLRNITRGAIRIEKNADLCYLST-IDWSL 159
Cdd:pfam01030   79 GLPSLKEITSGGVYIHNNPKLCYSETeIDWKL 110
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1004-1398 1.41e-19

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 92.50  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1004 RELGQGSFGMVYEGvakgvvkdEPETRVAIKTVNEAAS--MRERIEFLNEASVMKEFNCH-HVVRLLGVVSQGQPTLVIM 1080
Cdd:COG0515     6 RKLGEGSFGEVYLA--------RDRKLVALKVLAKKLEskSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1081 ELMTRGDLKSYLRSlrpevepRLSWNSLrrpgwprtlrdslasvsqvlalkqnnlvlippSLSKMIQMAGEIADGMAYLN 1160
Cdd:COG0515    78 EYVDGGSLEDLLKK-------IGRKGPL--------------------------------SESEALFILAQILSALEYLH 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1161 ANKFVHRDLAARNCMV-AEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPV----RWMSPESLKDGVF---TTHSDVWSFG 1232
Cdd:COG0515   119 SKGIIHRDIKPENILLdRDGRVVKLIDFGLAKLLPDPGSTSSIPALPSTSvgtpGYMAPEVLLGLSLayaSSSSDIWSLG 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1233 VVLWEIATlAEQPYQGLSN----EQVLRFVMEGGL--------LDKPDNCPDMLFELMRMCWQYNPKMRPsfleiigSIK 1300
Cdd:COG0515   199 ITLYELLT-GLPPFEGEKNssatSQTLKIILELPTpslasplsPSNPELISKAASDLLKKLLAKDPKNRL-------SSS 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1301 DEMEPSFQEVSFYYSEENKPPEPEELEMEPENMESVPLDPSASSASLPLPERHSGHKAENGPGPGVLVLRASFDErQPYA 1380
Cdd:COG0515   271 SDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSP-HNSS 349
                         410
                  ....*....|....*...
gi 568947361 1381 HMNGGRANERALPLPQSS 1398
Cdd:COG0515   350 SLLLSTASSKRSSLPKIS 367
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
230-277 1.82e-11

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 60.23  E-value: 1.82e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568947361  230 CCHPECLGsCHTPDdNTTCVACRHYYYK--GVCVPACPPGTYR-FEGWRCV 277
Cdd:cd00064     1 PCHPSCAT-CTGPG-PDQCTSCRHGFYLdgGTCVSECPEGTYAdTEGGVCL 49
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1159-1296 4.22e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 63.50  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1159 LNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEI 1238
Cdd:PTZ00267  185 VHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYEL 264
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947361 1239 ATLaEQPYQGLSNEQVLRFVMEGglldKPDNCP----DMLFELMRMCWQYNPKMRPSFLEII 1296
Cdd:PTZ00267  265 LTL-HRPFKGPSQREIMQQVLYG----KYDPFPcpvsSGMKALLDPLLSKNPALRPTTQQLL 321
FU smart00261
Furin-like repeats;
227-269 1.39e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.44  E-value: 1.39e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568947361    227 NNEC--CHPECLGsCHTPDdNTTCVACRHYYYK--GVCVPACPPGTY 269
Cdd:smart00261    1 DGECkpCHPECAT-CTGPG-PDDCTSCKHGFFLdgGKCVSECPPGTY 45
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
836-925 2.06e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  836 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYgGAKLNRLNPG-NYTARIQATSLSGN 914
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGtEYEFRVRAVNGGGE 82
                          90
                  ....*....|.
gi 568947361  915 GSWTDPVFFYV 925
Cdd:cd00063    83 SPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
836-917 2.44e-07

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 49.33  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   836 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKY---GSQVEDQRECVSRQEYRkyggAKLNRLNPG-NYTARIQATSL 911
Cdd:pfam00041    3 PTNLSVTDVTSTSLTVSWTPPPDGNGPITGYRVEYrpvNGGEPWNEITVPGTTTS----VTLTGLRPGtEYEVRVQAVNG 78

                   ....*.
gi 568947361   912 SGNGSW 917
Cdd:pfam00041   79 GGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
836-915 7.13e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 7.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361    836 PGPVTWEPRPENSIFLKW--PEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYggaKLNRLNPG-NYTARIQATSLS 912
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSY---TLTGLKPGtEYEFRVRAVNGA 80

                    ...
gi 568947361    913 GNG 915
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
494-607 1.21e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.88  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  494 LRFTSTTtwKNRIIITWHRyRPPDYRDLISFTVYYKEApfknvteydgqdacGSNSWNMVDVDLPPNKEgepgILLHGLK 573
Cdd:cd00063     7 LRVTDVT--STSVTLSWTP-PEDDGGPITGYVVEYREK--------------GSGDWKEVEVTPGSETS----YTLTGLK 65
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568947361  574 PWTQYAVYVKAVtltmveNDHIRGAKSEILYIRT 607
Cdd:cd00063    66 PGTEYEFRVRAV------NGGGESPPSESVTVTT 93
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
1030-1254 2.31e-06

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 52.15  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1030 RVAIKTVNEAA--SMRERIEFLNEASVMKEFNCHHVVRLLGvvsqgqptlvimelmtrgdlksylrslRPEVEPRLSWNS 1107
Cdd:TIGR03903    5 EVAIKLLRTDApeEEHQRARFRRETALCARLYHPNIVALLD---------------------------SGEAPPGLLFAV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1108 LRR-PGwpRTLRDSLASVSQVLALKQNNLVLippslskmiqmagEIADGMAYLNANKFVHRDLAARNCMVAE-DFT--VK 1183
Cdd:TIGR03903   58 FEYvPG--RTLREVLAADGALPAGETGRLML-------------QVLDALACAHNQGIVHRDLKPQNIMVSQtGVRphAK 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1184 IGDFGM------TRDIYETDYYRKgGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEI---------ATLAEQPYQG 1248
Cdd:TIGR03903  123 VLDFGIgtllpgVRDADVATLTRT-TEVLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECltgqrvvqgASVAEILYQQ 201

                   ....*.
gi 568947361  1249 LSNEQV 1254
Cdd:TIGR03903  202 LSPVDV 207
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-586 2.14e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 2.14e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361    494 LRFTSTTtwKNRIIITWhryRPPDYRDLISFTVYYKEapfknvtEYDGQDAcgsnSWNMVDVDLPPNKegepgILLHGLK 573
Cdd:smart00060    7 LRVTDVT--STSVTLSW---EPPPDDGITGYIVGYRV-------EYREEGS----EWKEVNVTPSSTS-----YTLTGLK 65
                            90
                    ....*....|...
gi 568947361    574 PWTQYAVYVKAVT 586
Cdd:smart00060   66 PGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
612-656 1.54e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 1.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947361  612 PSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDG 656
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD 45
fn3 pfam00041
Fibronectin type III domain;
494-586 1.76e-03

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 38.54  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   494 LRFTSTTTwkNRIIITWhryRPPDYR--DLISFTVYYKEApfknvteyDGQDAcgsnsWNMVDVDLPPNkegepGILLHG 571
Cdd:pfam00041    6 LSVTDVTS--TSLTVSW---TPPPDGngPITGYRVEYRPV--------NGGEP-----WNEITVPGTTT-----SVTLTG 62
                           90
                   ....*....|....*
gi 568947361   572 LKPWTQYAVYVKAVT 586
Cdd:pfam00041   63 LRPGTEYEVRVQAVN 77
 
Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
993-1301 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 566.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  993 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1072
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1073 GQPTLVIMELMTRGDLKSYLRSLRPEVEprlswnslrrpgwprtlrdslasvsqvlalkqNNLVLIPPSLSKMIQMAGEI 1152
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAE--------------------------------NNPGLGPPTLQKFIQMAAEI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1153 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFG 1232
Cdd:cd05032   129 ADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFG 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947361 1233 VVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1301
Cdd:cd05032   209 VVLWEMATLAEQPYQGLSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
993-1312 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 563.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  993 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1072
Cdd:cd05061     1 WEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1073 GQPTLVIMELMTRGDLKSYLRSLRPEVEprlswnslRRPGWPrtlrdslasvsqvlalkqnnlvliPPSLSKMIQMAGEI 1152
Cdd:cd05061    81 GQPTLVVMELMAHGDLKSYLRSLRPEAE--------NNPGRP------------------------PPTLQEMIQMAAEI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1153 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFG 1232
Cdd:cd05061   129 ADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1233 VVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKDEMEPSFQEVSF 1312
Cdd:cd05061   209 VVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSF 288
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
993-1301 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 549.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  993 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1072
Cdd:cd05062     1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1073 GQPTLVIMELMTRGDLKSYLRSLRPEVEprlswnslrrpgwprtlrdslasvsqvlalkqNNLVLIPPSLSKMIQMAGEI 1152
Cdd:cd05062    81 GQPTLVIMELMTRGDLKSYLRSLRPEME--------------------------------NNPVQAPPSLKKMIQMAGEI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1153 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFG 1232
Cdd:cd05062   129 ADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFG 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947361 1233 VVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1301
Cdd:cd05062   209 VVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKE 277
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
1000-1296 8.83e-129

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 398.02  E-value: 8.83e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1000 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1079
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGE-GENTKIKVAVKTLKEGADEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1080 MELMTRGDLKSYLRSLRPeveprlswnslrrpgwprtlrdslasvsqvlalkqnnlvliPPSLSKMIQMAGEIADGMAYL 1159
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHKG-----------------------------------------KLTLKDLLSMALQIAKGMEYL 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  1160 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIA 1239
Cdd:pfam07714  119 ESKNFVHRDLAARNILVTENLVVKISDFGLSRDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIF 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947361  1240 TLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 1296
Cdd:pfam07714  199 TLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMTQCWAYDPEDRPTFSELV 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1004-1296 2.75e-128

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 396.91  E-value: 2.75e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1004 RELGQGSFGMVYEGVAKGvvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELM 1083
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKG--GDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1084 TRGDLKSYLRSlrpeveprlswnslRRPGWPRTLRDSLasvsqvlalkqnnlvlippSLSKMIQMAGEIADGMAYLNANK 1163
Cdd:cd00192    79 EGGDLLDFLRK--------------SRPVFPSPEPSTL-------------------SLKDLLSFAIQIAKGMEYLASKK 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1164 FVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAE 1243
Cdd:cd00192   126 FVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGA 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568947361 1244 QPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 1296
Cdd:cd00192   206 TPYPGLSNEEVLEYLRKGYRLPKPENCPDELYELMLSCWQLDPEDRPTFSELV 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1000-1299 1.13e-120

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 376.12  E-value: 1.13e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1000 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1079
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGK-GDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1080 MELMTRGDLKSYLRSLRPEVeprlswnslrrpgwprtlrdslasvsqvlalkqnnlvlipPSLSKMIQMAGEIADGMAYL 1159
Cdd:smart00221   80 MEYMPGGDLLDYLRKNRPKE----------------------------------------LSLSDLLSFALQIARGMEYL 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1160 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGkGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIA 1239
Cdd:smart00221  120 ESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF 198
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1240 TLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSI 1299
Cdd:smart00221  199 TLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1000-1296 2.90e-120

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 374.95  E-value: 2.90e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1000 ITMNRELGQGSFGMVYEGVAKGVVKDEPETrVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1079
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVE-VAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1080 MELMTRGDLKSYLRSLRPEVeprlswnslrrpgwprtlrdslasvsqvlalkqnnlvlippSLSKMIQMAGEIADGMAYL 1159
Cdd:smart00219   80 MEYMEGGDLLSYLRKNRPKL-----------------------------------------SLSDLLSFALQIARGMEYL 118
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361   1160 NANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGkGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIA 1239
Cdd:smart00219  119 ESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRKRG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF 197
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947361   1240 TLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 1296
Cdd:smart00219  198 TLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELV 254
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1006-1301 1.08e-109

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 347.10  E-value: 1.08e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1006 LGQGSFGMVYEGVAKGVVKD-EPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMT 1084
Cdd:cd05044     3 LGSGAFGEVFEGTAKDILGDgSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1085 RGDLKSYLRSLRPEVEPrlswnslrrpgwprtlrdslasvsqvlalkqnnlvliPP--SLSKMIQMAGEIADGMAYLNAN 1162
Cdd:cd05044    83 GGDLLSYLRAARPTAFT-------------------------------------PPllTLKDLLSICVDVAKGCVYLEDM 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1163 KFVHRDLAARNCMVAE----DFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEI 1238
Cdd:cd05044   126 HFVHRDLAARNCLVSSkdyrERVVKIGDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEI 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947361 1239 ATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1301
Cdd:cd05044   206 LTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQN 268
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
994-1300 3.38e-100

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 321.26  E-value: 3.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  994 EVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 1073
Cdd:cd05036     2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1074 QPTLVIMELMTRGDLKSYLRSLRPeveprlswnslrRPGWPRTLrdslasvsqvlalkqnnlvlippSLSKMIQMAGEIA 1153
Cdd:cd05036    82 LPRFILLELMAGGDLKSFLRENRP------------RPEQPSSL-----------------------TMLDLLQLAQDVA 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1154 DGMAYLNANKFVHRDLAARNCMVA---EDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWS 1230
Cdd:cd05036   127 KGCRYLEENHFIHRDIAARNCLLTckgPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWS 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1231 FGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIK 1300
Cdd:cd05036   207 FGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
994-1295 3.28e-90

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 294.05  E-value: 3.28e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  994 EVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 1073
Cdd:cd05050     1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1074 QPTLVIMELMTRGDLKSYLRSLRPEVEPRLSWNS--LRRPGWPrtlrdslasvsqvlalkqnnlvliPPSLSKMIQ--MA 1149
Cdd:cd05050    81 KPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTssARKCGLN------------------------PLPLSCTEQlcIA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1150 GEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVW 1229
Cdd:cd05050   137 KQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVW 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947361 1230 SFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 1295
Cdd:cd05050   217 AYGVVLWEIFSYGMQPYYGMAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
994-1295 1.60e-88

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 288.98  E-value: 1.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  994 EVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 1073
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1074 QPTLVIMELMTRGDLKSYLRSLRPEveprlswnslrrpgwprtlrdslasvsqVLALKQNNLVLIPPSLSKMIQMAGEIA 1153
Cdd:cd05049    81 DPLLMVFEYMEHGDLNKFLRSHGPD----------------------------AAFLASEDSAPGELTLSQLLHIAVQIA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361 1154 DGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGV 1233
Cdd:cd05049   133 SGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGV 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947361 1234 VLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 1295
Cdd:cd05049   213 VLWEIFTYGKQPWFQLSNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
992-1296 2.81e-87

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 285.85  E-value: 2.81e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947361  992 EWEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPET-RVAIKTVNEAASMRERIEFLNEASVMKEFNCH-HVVRLLG